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The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12. Specific Inactivation of the Homoserine Dehydrogenase Activity by the Affinity Label, 2-Amino-4-oxo-5-chloropentanoic Acid
| Content Provider | Scilit |
|---|---|
| Author | Hirth, Christian G. Veron, Michel Villar-Palasi, Carlos Hurion, Nicole Cohen, Georges N. |
| Copyright Year | 1975 |
| Description | Journal: Journal of Biological Inorganic Chemistry 2-Amino-4-oxo-5-chloropentanoic acid inactivates specifically the homoserine dehydrogenase activity of the bifunctional enzyme, aspartokinase I--homoserine dehydrogenase I. The aspartokinase activity remains essentially untouched and retains its threonine sensitivity. The inactivation of the dehydrogenase requires the covalent binding of one equivalent of the analogue per subunit. Alkylation does not affect the tetrameric state of the protein. The alkylating agent, a substrate analogue, meets the qualitative and quantitative requirements of an affinity label. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1975.tb09819.x/pdf |
| Ending Page | 430 |
| Page Count | 6 |
| Starting Page | 425 |
| ISSN | 09498257 |
| e-ISSN | 14321327 |
| DOI | 10.1111/j.1432-1033.1975.tb09819.x |
| Journal | Journal of Biological Inorganic Chemistry |
| Issue Number | 2 |
| Volume Number | 50 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1975-01-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Homoserine Dehydrogenase |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |